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Protein

Ribulose bisphosphate carboxylase small chain 1A, chloroplastic

Gene

RBCS-1A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (By similarity).By similarity

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

GO - Molecular functioni

  1. copper ion binding Source: TAIR
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. chloroplast ribulose bisphosphate carboxylase complex biogenesis Source: TAIR
  2. photorespiration Source: UniProtKB-KW
  3. photosynthesis Source: TAIR
  4. reductive pentose-phosphate cycle Source: UniProtKB-KW
  5. response to blue light Source: TAIR
  6. response to cold Source: TAIR
  7. response to far red light Source: TAIR
  8. response to red light Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Enzyme and pathway databases

BioCyciARA:GQT-1261-MONOMER.
MetaCyc:AT1G67090-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase small chain 1A, chloroplastic (EC:4.1.1.39)
Short name:
RuBisCO small subunit 1A
Gene namesi
Name:RBCS-1A
Synonyms:ATS1A
Ordered Locus Names:At1g67090
ORF Names:F1O19.14, F5A8.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G67090.

Subcellular locationi

Plastidchloroplast membrane 1 Publication; Peripheral membrane protein 1 Publication. Plastidchloroplast stroma 1 Publication

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. chloroplast envelope Source: TAIR
  4. chloroplast membrane Source: UniProtKB-SubCell
  5. chloroplast stroma Source: TAIR
  6. chloroplast thylakoid membrane Source: TAIR
  7. cytosolic ribosome Source: TAIR
  8. membrane Source: TAIR
  9. thylakoid Source: TAIR
  10. thylakoid lumen Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555ChloroplastAdd
BLAST
Chaini56 – 180125Ribulose bisphosphate carboxylase small chain 1A, chloroplasticPRO_0000031463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP10795.
PRIDEiP10795.

2D gel databases

World-2DPAGE0003:P10795.

Expressioni

Gene expression databases

ExpressionAtlasiP10795. baseline.
GenevestigatoriP10795.

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Protein-protein interaction databases

BioGridi28250. 5 interactions.
IntActiP10795. 6 interactions.
MINTiMINT-2584041.

Structurei

3D structure databases

ProteinModelPortaliP10795.
SMRiP10795. Positions 56-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
InParanoidiP10795.
KOiK01602.
OMAiAFPATRK.
PhylomeDBiP10795.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P10795-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASSMLSSAT MVASPAQATM VAPFNGLKSS AAFPATRKAN NDITSITSNG
60 70 80 90 100
GRVNCMQVWP PIGKKKFETL SYLPDLTDSE LAKEVDYLIR NKWIPCVEFE
110 120 130 140 150
LEHGFVYREH GNSPGYYDGR YWTMWKLPLF GCTDSAQVLK EVEECKKEYP
160 170 180
NAFIRIIGFD NTRQVQCISF IAYKPPSFTG
Length:180
Mass (Da):20,216
Last modified:January 10, 2003 - v2
Checksum:i5DE768676D61F8F7
GO

Sequence cautioni

The sequence AAK49590.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA31948.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151G → R in AAG40356 (PubMed:14593172).Curated
Sequence conflicti171 – 1711I → V in CAA31948 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13611 Genomic DNA. Translation: CAA31948.1. Sequence problems.
AC004146 Genomic DNA. Translation: AAD10655.1.
AC007152 Genomic DNA. No translation available.
CP002684 Genomic DNA. Translation: AEE34594.1.
AF325011 mRNA. Translation: AAG40363.1.
AF325004 mRNA. Translation: AAG40356.1.
AF372874 mRNA. Translation: AAK49590.1. Different initiation.
AF410291 mRNA. Translation: AAK95277.1.
AY054188 mRNA. Translation: AAL06849.1.
AY054581 mRNA. Translation: AAK96772.1.
AY058831 mRNA. Translation: AAL24219.1.
AY059940 mRNA. Translation: AAL24422.1.
AY062612 mRNA. Translation: AAL32690.1.
AY062711 mRNA. Translation: AAL32789.1.
AY065101 mRNA. Translation: AAL38277.1.
AY093380 mRNA. Translation: AAM13379.1.
AY093388 mRNA. Translation: AAM13387.1.
AY097366 mRNA. Translation: AAM19882.1.
BT000362 mRNA. Translation: AAN15681.1.
BT002076 mRNA. Translation: AAN72087.1.
X68342 Other DNA. Translation: CAA48415.1. Different termination.
PIRiG96694.
S03720. RKMUA1.
RefSeqiNP_176880.1. NM_105379.3. [P10795-1]
UniGeneiAt.12721.
At.30194.
At.37531.
At.46639.
At.49098.
At.67454.
At.68122.
At.70032.
At.70053.

Genome annotation databases

EnsemblPlantsiAT1G67090.1; AT1G67090.1; AT1G67090. [P10795-1]
GeneIDi843029.
KEGGiath:AT1G67090.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13611 Genomic DNA. Translation: CAA31948.1. Sequence problems.
AC004146 Genomic DNA. Translation: AAD10655.1.
AC007152 Genomic DNA. No translation available.
CP002684 Genomic DNA. Translation: AEE34594.1.
AF325011 mRNA. Translation: AAG40363.1.
AF325004 mRNA. Translation: AAG40356.1.
AF372874 mRNA. Translation: AAK49590.1. Different initiation.
AF410291 mRNA. Translation: AAK95277.1.
AY054188 mRNA. Translation: AAL06849.1.
AY054581 mRNA. Translation: AAK96772.1.
AY058831 mRNA. Translation: AAL24219.1.
AY059940 mRNA. Translation: AAL24422.1.
AY062612 mRNA. Translation: AAL32690.1.
AY062711 mRNA. Translation: AAL32789.1.
AY065101 mRNA. Translation: AAL38277.1.
AY093380 mRNA. Translation: AAM13379.1.
AY093388 mRNA. Translation: AAM13387.1.
AY097366 mRNA. Translation: AAM19882.1.
BT000362 mRNA. Translation: AAN15681.1.
BT002076 mRNA. Translation: AAN72087.1.
X68342 Other DNA. Translation: CAA48415.1. Different termination.
PIRiG96694.
S03720. RKMUA1.
RefSeqiNP_176880.1. NM_105379.3. [P10795-1]
UniGeneiAt.12721.
At.30194.
At.37531.
At.46639.
At.49098.
At.67454.
At.68122.
At.70032.
At.70053.

3D structure databases

ProteinModelPortaliP10795.
SMRiP10795. Positions 56-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi28250. 5 interactions.
IntActiP10795. 6 interactions.
MINTiMINT-2584041.

2D gel databases

World-2DPAGE0003:P10795.

Proteomic databases

PaxDbiP10795.
PRIDEiP10795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G67090.1; AT1G67090.1; AT1G67090. [P10795-1]
GeneIDi843029.
KEGGiath:AT1G67090.

Organism-specific databases

TAIRiAT1G67090.

Phylogenomic databases

eggNOGiCOG4451.
HOGENOMiHOG000141332.
InParanoidiP10795.
KOiK01602.
OMAiAFPATRK.
PhylomeDBiP10795.

Enzyme and pathway databases

BioCyciARA:GQT-1261-MONOMER.
MetaCyc:AT1G67090-MONOMER.

Gene expression databases

ExpressionAtlasiP10795. baseline.
GenevestigatoriP10795.

Family and domain databases

Gene3Di3.30.190.10. 1 hit.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
IPR024680. RuBisCO_ssu_N.
[Graphical view]
PfamiPF12338. RbcS. 1 hit.
PF00101. RuBisCO_small. 1 hit.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 1 hit.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Four genes in two diverged subfamilies encode the ribulose-1,5-bisphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana."
    Krebbers E., Seurinck J., Herdies L., Cashmore A.R., Timko M.P.
    Plant Mol. Biol. 11:745-759(1987)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: cv. Columbia K85.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Arabidopsis thaliana small subunit leader and transit peptide enhance the expression of Bacillus thuringiensis proteins in transgenic plants."
    Wong E.Y., Hironaka C.M., Fishhoff D.A.
    Plant Mol. Biol. 20:81-93(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-79.
  6. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRBS1A_ARATH
AccessioniPrimary (citable) accession number: P10795
Secondary accession number(s): Q94JW2, Q9FPI6, Q9SAV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 10, 2003
Last modified: January 7, 2015
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are four genes coding for RBS in Arabidopsis thaliana.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.